FLDA_CLOSG
ID FLDA_CLOSG Reviewed; 412 AA.
AC Q93AM1;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Cinnamoyl-CoA:phenyllactate CoA-transferase {ECO:0000303|PubMed:10849007, ECO:0000303|PubMed:11967068};
DE EC=2.8.3.17 {ECO:0000269|PubMed:10849007, ECO:0000305|PubMed:11967068};
DE AltName: Full=(E)-cinnamoyl-CoA:(R)-phenyllactate CoA-transferase;
DE AltName: Full=(R)-phenyllactate CoA-transferase {ECO:0000303|PubMed:11967068};
GN Name=fldA {ECO:0000303|PubMed:10849007, ECO:0000303|PubMed:11967068};
OS Clostridium sporogenes.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1509;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBUNIT.
RC STRAIN=ATCC 3584;
RX PubMed=11967068; DOI=10.1046/j.1365-2958.2002.02867.x;
RA Dickert S., Pierik A.J., Buckel W.;
RT "Molecular characterization of phenyllactate dehydratase and its initiator
RT from Clostridium sporogenes.";
RL Mol. Microbiol. 44:49-60(2002).
RN [2]
RP PROTEIN SEQUENCE OF 1-39, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, MASS SPECTROMETRY, SUBSTRATE SPECIFICITY, SUBUNIT, AND PATHWAY.
RC STRAIN=ATCC 3584;
RX PubMed=10849007; DOI=10.1046/j.1432-1327.2000.01427.x;
RA Dickert S., Pierik A.J., Linder D., Buckel W.;
RT "The involvement of coenzyme A esters in the dehydration of (R)-
RT phenyllactate to (E)-cinnamate by Clostridium sporogenes.";
RL Eur. J. Biochem. 267:3874-3884(2000).
CC -!- FUNCTION: Component of the phenyllactate dehydratase complex FldABC
CC that is involved in the fermentation of L-phenylalanine via a Stickland
CC reaction. This complex catalyzes the reversible syn-dehydration of (R)-
CC phenyllactate to (E)-cinnamate in two steps, a CoA-transfer from
CC cinnamoyl-CoA to phenyllactate, catalyzed by FldA, followed by the
CC dehydration of phenyllactyl-CoA to cinnamoyl-CoA, catalyzed by FldB and
CC FldC (PubMed:10849007, PubMed:11967068). In vitro, FldA can use 3-
CC phenylpropanoate as a better CoA-acceptor than phenyllactate
CC (PubMed:10849007). {ECO:0000269|PubMed:10849007,
CC ECO:0000269|PubMed:11967068}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-cinnamoyl-CoA + (R)-3-phenyllactate = (E)-cinnamate + (R)-
CC 3-phenyllactoyl-CoA; Xref=Rhea:RHEA:15601, ChEBI:CHEBI:11009,
CC ChEBI:CHEBI:15669, ChEBI:CHEBI:57252, ChEBI:CHEBI:57254; EC=2.8.3.17;
CC Evidence={ECO:0000269|PubMed:10849007, ECO:0000305|PubMed:11967068};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3 uM for (E)-cinnamoyl-CoA (at pH 7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:10849007};
CC KM=9 uM for 3-phenylpropanoate (at pH 7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:10849007};
CC Vmax=5.3 umol/min/mg enzyme with (E)-cinnamoyl-CoA and 3-
CC phenylpropanoate as substrates (at pH 7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:10849007};
CC pH dependence:
CC Optimum pH is between 7 and 8. {ECO:0000269|PubMed:10849007};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:10849007};
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation.
CC {ECO:0000305|PubMed:10849007}.
CC -!- SUBUNIT: Homodimer (PubMed:10849007). Part of the heterotrimeric
CC phenyllactate dehydratase complex FldABC, composed of (R)-phenyllactate
CC CoA-transferase (FldA) and a heterodimeric (R)-phenyllactyl-CoA
CC dehydratase (FldB and FldC) (PubMed:10849007, PubMed:11967068).
CC {ECO:0000269|PubMed:10849007, ECO:0000269|PubMed:11967068}.
CC -!- MASS SPECTROMETRY: Mass=46440; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10849007};
CC -!- SIMILARITY: Belongs to the CoA-transferase III family. {ECO:0000305}.
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DR EMBL; AF420489; AAL18808.1; -; Genomic_DNA.
DR AlphaFoldDB; Q93AM1; -.
DR SMR; Q93AM1; -.
DR KEGG; ag:AAL18808; -.
DR BioCyc; MetaCyc:MON-20598; -.
DR SABIO-RK; Q93AM1; -.
DR UniPathway; UPA00139; -.
DR GO; GO:0043785; F:cinnamoyl-CoA:phenyllactate CoA-transferase activity; IDA:UniProtKB.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006558; P:L-phenylalanine metabolic process; IDA:UniProtKB.
DR Gene3D; 3.30.1540.10; -; 1.
DR Gene3D; 3.40.50.10540; -; 1.
DR InterPro; IPR003673; CoA-Trfase_fam_III.
DR InterPro; IPR044855; CoA-Trfase_III_dom3_sf.
DR InterPro; IPR023606; CoA-Trfase_III_dom_1_sf.
DR Pfam; PF02515; CoA_transf_3; 1.
DR SUPFAM; SSF89796; SSF89796; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Transferase.
FT CHAIN 1..412
FT /note="Cinnamoyl-CoA:phenyllactate CoA-transferase"
FT /id="PRO_0000422996"
FT ACT_SITE 176
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
SQ SEQUENCE 412 AA; 46387 MW; C1FD47C358DD4014 CRC64;
MENNTNMFSG VKVIELANFI AAPAAGRFFA DGGAEVIKIE SPAGDPLRYT APSEGRPLSQ
EENTTYDLEN ANKKAIVLNL KSEKGKKILH EMLAEADILL TNWRTKALVK QGLDYETLKE
KYPKLVFAQI TGYGEKGPDK DLPGFDYTAF FARGGVSGTL YEKGTVPPNV VPGLGDHQAG
MFLAAGMAGA LYKAKTTGQG DKVTVSLMHS AMYGLGIMIQ AAQYKDHGLV YPINRNETPN
PFIVSYKSKD DYFVQVCMPP YDVFYDRFMT ALGREDLVGD ERYNKIENLK DGRAKEVYSI
IEQQMVTKTK DEWDNIFRDA DIPFAIAQTW EDLLEDEQAW ANDYLYKMKY PTGNERALVR
LPVFFKEAGL PEYNQSPQIA ENTVEVLKEM GYTEQEIEEL EKDKDIMVRK EK
